Peroxycarboxylic acids (“peracids”) are effective antimicrobial agents. Methods to clean, disinfect, and/or sanitize hard surfaces, food products, living plant tissues, and medical devices against undesirable microbial growth have been described (e.g., U.S. Pat. No. 6,545,047; U.S. Pat. No. 6,183,807; U.S. Pat. No. 6,518,307; U.S. Pat. No. 5,683,724; and U.S. Pat. No. 6,635,286). Peracids have also been reported to be useful in preparing bleaching compositions for laundry detergent applications (e.g., U.S. Pat. No. 3,974,082; U.S. Pat. No. 5,296,161; and U.S. Pat. No. 5,364,554).
Oral care compositions comprising a peracid have also been disclosed. U.S. Pat. No. 5,302,375 to Viscio, D., discloses oral compositions for whitening teeth comprising peracetic acid dissolved in a vehicle, wherein the peracetic acid is generated within the vehicle in situ by combining water, acetylsalicylic acid, and a water soluble alkali metal percarbonate. U.S. Pat. No. 5,279,816 to Church et al. discloses the use of a composition comprising peracetic acid to whiten stained or discolored teeth. U.S. Pat. Nos. 6,221,341 and 7,189,385 to Montgomery, R., disclose peroxy acid tooth-whitening compositions suitable for use in a method to whiten teeth. More specifically, a peracetic acid composition is produced by combining a hydrogen peroxide precursor, an acetic acid ester of glycerin, and water to generate, via chemical perhydrolysis, peracetic acid. Enzymatic perhydrolysis is not described.
U.S. Patent Application Publication No. 2009-0311198 to Concar et al. discloses an oral composition comprising an M. smegmatis enzyme having perhydrolytic activity to bleach teeth. The use of a CE-7 perhydrolase to produce a peracid benefit agent is not disclosed. Concar et al. is also silent on the use of a targeted perhydrolytic enzyme in an oral care composition.
The inclusion of specific variant subtilisin Carlsberg proteases having perhydrolytic activity in a body care product is disclosed in U.S. Pat. No. 7,510,859 to Wieland et al. Perhydrolytic enzymes beyond the specific variant proteases are not described nor are there any working examples demonstrating the enzymatic production of peracid as a personal care benefit agent.
U.S. Patent Application Publication Nos. 2008-0176783 A1; 2008-0176299 A1; 2009-0005590 A1; and 2010-0041752 A1 to DiCosimo et al. disclose enzymes structurally classified as members of the CE-7 family of carbohydrate esterases (i.e., cephalosporin C deacetylases [CAHs] and acetyl xylan esterases [AXEs]) that are characterized by significant perhydrolytic activity for converting carboxylic acid ester substrates (in the presence of a suitable source of peroxygen, such as hydrogen peroxide) into peroxycarboxylic acids at concentrations sufficient for use as a disinfectant and/or a bleaching agent. Some members of the CE-7 family of carbohydrate esterases have been demonstrated to have perhydrolytic activity sufficient to produce 4000-5000 ppm peracetic acid from acetyl esters of alcohols, diols, and glycerols in 1 minute and up to 9000 ppm between 5 minutes and 30 minutes once the reaction components were mixed (DiCosimo et al., U.S. 2009-0005590 A1). U.S. Patent application publication No. 2010-0087529 A1 describes variant CE-7 enzymes having improved perhydrolytic activity. Although the CE-7 perhydrolases have exceptional perhydrolytic activity, their use in personal care products has not been disclosed. As such, a problem to be solved is to provide personal care compositions and methods comprising the use of at least one CE-7 perhydrolase for the production of a peracid benefit agent.
Peracids are strong oxidizing agents that may be reactive towards a variety of materials, including materials not targeted for the desired benefit. As such, certain personal care applications may benefit from the ability to target/focus the peracid benefit agent to the desired body surface by localizing peracid production on or near the desired target body surface. Enzymatic peracid production may benefit by targeting the perhydrolase to the body surface. An additional benefit can be achieved by targeting the perhydrolase to a delivery material so as to limit enzyme concentration and exposure of the user.
Oral care compositions and/or methods of treating an oral care surface with an enzyme coupled to an oral cavity material have been reported. U.S. Pat. No. 4,138,476 to Simonson et al. discloses a process for treating plaque comprising the use of a glucan-degrading enzyme covalently coupled, via a complexing reagent, to a phosphate carrier group having affinity for the surface of a tooth. The enzymatic degradation of the glucan deposits is said to promote dissolution and dispersion of plaque material.
U.S. Patent Application Publication No. 2005-0158253, U.S. Pat. No. 6,830,745 to Budny et al. discloses a two-component composition comprising an anchor enzyme complex to enzymatically degrade biofilm structures and a second anchor enzyme component capable of acting directly upon bacteria. The biofilm-degrading enzymes are those that directly degrade the exopolysaccharide backbone structures.
U.S. Pat. No. 5,871,714 to Budny, J., discloses a composition for controlling bacterial growth/colonization (e.g., reducing dental plaque) comprising an enzyme that degrades the plaque matrix coupled to an anchor molecule. The use of a targeted perhydrolase is not disclosed.
U.S. Pat. No. 5,490,988 and EP 0479,600 B1 to Beggs et al. discloses the use of antibody fragments as a means for binding to a target site, wherein a therapeutic agent is connected through an additional peptide appended to the antibody fragment to attach the therapeutic agent to the target site. An oral care product is disclosed comprising a modified antibody fragment having affinity to an antigentic component of bacteria in dental plaque to delivery a therapeutic agent. The therapeutic agent may be a cytotoxic agent produced by an enzyme or a combination of enzymes, such as an oxidase in combination with a peroxidase to form oxidized halides. The use of a targeted perhydrolase to produce a peracid benefit agent is not described.
EP 0450,800 B1 to Beggs et al, discloses the utilization of two different enzymes working together to attack species occurring in the oral microflora. The first enzyme generates an intermediate product that is used as a substrate for the second enzyme to produce an agent active against a target within the mouth. Each enzyme is attached to an antibody or antibody fragment having affinity to a target surface within the mouth, whereby in use the enzymes are coupled to the target site in proximity to each other. Exemplified is a combination of a glucose oxidase to produce hydrogen peroxide which then may be converted by a peroxidase, in the presence of a halide or thiocyanate, to produce a hypohalite or hypothiocyanate, respectively. The use of a targeted perhydrolase to produce a peracid benefit agent is not described.
EP 0451,972 B1 to Beggs et al. describes a product comprising a two enzymes, the product comprising a first enzyme for generating an active agent against a target and a second enzyme for generating an intermediate which is a substrate for the first enzyme; said product further comprising a linking means (i.e., an antibody or antibody fragment) attached or attachable to both enzymes to couple the enzymes together, thereby forming a complex which binds to a target cell. Exemplified is an oxidase (capable of generating hydrogen peroxide) coupled to a peroxidase which catalyzes the formation of a hypohalite or hypothiocyanate active agent.
EP 0453,097 B1 to Beggs et al. describes the delivery of an active agent to a target site using a plurality of antibodies or antibody fragments which can self assemble to form a bridge between the agent and the target site. The active agent is glucose oxidase or a combination of a glucose oxidase and a peroxidase. The use of targeted perhydrolase to produce a peracid benefit agent is not described.
The use of antibodies, antibody fragments (Fab), single chain fused variable region antibodies (scFc), Camelidae antibodies, and large scaffold display proteins as peptidic affinity materials may not be suitable for some personal care applications due to their size and cost. As such, there remains a need in certain low cost cosmetic applications to use shorter, less expensive peptidic affinity materials for targeted delivery of a benefit agent.
The use of shorter, biopanned peptides having strong affinity for a body surface to target a cosmetic benefit agent to a body surface has been described (U.S. Pat. Nos. 7,220,405; 7,309,482; 7,285,264 and 7,807,141; U.S. Patent Application Publication Nos. 2005-0226839 A1; 2007-0196305 A1; 2006-0199206 A1; 2007-0065387 A1; 2008-0107614 A1; 2007-0110686 A1; 2006-0073111 A1; 2010-0158846; 2010-0158847; and 2010-0247589; and published PCT applications WO2008/054746; WO2004/048399, and WO2008/073368). U.S. Pat. No. 7,807,141 to Huang et al. discloses peptide-based oral care surface reagents suitable to couple an oral care benefit agent to a tooth surface. The use of a peptidic material having affinity for an oral cavity surface to couple an active CE-7 perhydrolase (i.e., “targeted perhydrolases”) for the production of a peracid benefit agent has not been described.
As such, an additional problem to be solved is to provide compositions and methods suitable to target enzymatic peracid production to an oral cavity surface.